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• W133905691 abstract "Research Article1 September 1994free access Solution structure of the LexA repressor DNA binding domain determined by 1H NMR spectroscopy. R.H. Fogh R.H. Fogh Bijvoet Center for Biomolecular Research, Utrecht University, The Netherlands. Search for more papers by this author G. Ottleben G. Ottleben Bijvoet Center for Biomolecular Research, Utrecht University, The Netherlands. Search for more papers by this author H. Rüterjans H. Rüterjans Bijvoet Center for Biomolecular Research, Utrecht University, The Netherlands. Search for more papers by this author M. Schnarr M. Schnarr Bijvoet Center for Biomolecular Research, Utrecht University, The Netherlands. Search for more papers by this author R. Boelens R. Boelens Bijvoet Center for Biomolecular Research, Utrecht University, The Netherlands. Search for more papers by this author R. Kaptein R. Kaptein Bijvoet Center for Biomolecular Research, Utrecht University, The Netherlands. Search for more papers by this author R.H. Fogh R.H. Fogh Bijvoet Center for Biomolecular Research, Utrecht University, The Netherlands. Search for more papers by this author G. Ottleben G. Ottleben Bijvoet Center for Biomolecular Research, Utrecht University, The Netherlands. Search for more papers by this author H. Rüterjans H. Rüterjans Bijvoet Center for Biomolecular Research, Utrecht University, The Netherlands. Search for more papers by this author M. Schnarr M. Schnarr Bijvoet Center for Biomolecular Research, Utrecht University, The Netherlands. Search for more papers by this author R. Boelens R. Boelens Bijvoet Center for Biomolecular Research, Utrecht University, The Netherlands. Search for more papers by this author R. Kaptein R. Kaptein Bijvoet Center for Biomolecular Research, Utrecht University, The Netherlands. Search for more papers by this author Author Information R.H. Fogh1, G. Ottleben1, H. Rüterjans1, M. Schnarr1, R. Boelens1 and R. Kaptein1 1Bijvoet Center for Biomolecular Research, Utrecht University, The Netherlands. The EMBO Journal (1994)13:3936-3944https://doi.org/10.1002/j.1460-2075.1994.tb06709.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info The structure of the 84 residue DNA binding domain of the Escherichia coli LexA repressor has been determined from NMR data using distance geometry and restrained molecular dynamics. The assignment of the 1H NMR spectrum of the molecule, derived from 2- and 3-D homonuclear experiments, is also reported. A total of 613 non-redundant distance restraints were used to give a final family of 28 structures. The structured region of the molecule consisted of residues 4-69 and yielded a r.m.s. deviation from an average of 0.9 A for backbone and 1.6 A for all heavy atoms. The structure contains three regular alpha-helices at residues 6-21 (I), 28-35 (II) and 41-52 (III), and an antiparallel beta-sheet at residues 56-58 and 66-68. Helices II and III form a variant helix-turn-helix DNA binding motif, with an unusual one residue insert at residue 38. The topology of the LexA DNA binding domain is found to be the same as for the DNA binding domains of the catabolic activator protein, human histone 5, the HNF-3/fork head protein and the Kluyveromyces lactis heat shock transcription factor. Previous ArticleNext Article Volume 13Issue 171 September 1994In this issue RelatedDetailsLoading ..." @default.
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• W133905691 date "1994-09-01" @default.
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• W133905691 title "Solution structure of the LexA repressor DNA binding domain determined by 1H NMR spectroscopy." @default.
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• W133905691 doi "https://doi.org/10.1002/j.1460-2075.1994.tb06709.x" @default.
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